› 1do8

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF A CLOSED FORM OF HUMAN MITOCHONDRIAL NAD(P)+-DEPENDENT MALIC ENZYME

Released:
DOI: 10.2210/pdb1do8/pdb
PDB entry 1do8 coloured by chain, front view.
PDB entry 1do8 coloured by chain, side view.
PDB entry 1do8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a closed form of human malic enzyme and implications for catalytic mechanism.
Yang Z, Floyd DL, Loeber G, Tong L
Nat Struct Biol 7 251-7 (2000)
PMID: 10700286

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = pyruvate + CO(2) + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149937 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent malic enzyme, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 564 amino acids
Theoretical weight: 63.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23368 (Residues: 21-584; Coverage: 97%)
Gene name: ME2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 8 x NAD
2 bound ligands:
Ligand OXL 4 x OXL
Ligand MN 4 x MN
1 modified residue:
Ligand MSE 56 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 229Å b: 118.7Å c: 113Å
α: 90° β: 109.6° γ: 90°
R-values:
R R work R free
0.214 0.204 0.263
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Malo-ethanolic fermentation in Saccharomyces and Schizosaccharomyces.
Volschenk et al. (2003)
46 other articles

5 mentions without citation

Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme).
Hung et al. (2005)
4 more